Abstract
L‐DOPA dioxygenase is part of a mini‐pathway to the synthon 3‐vinyl‐2,3‐pyrroline‐5‐carboxylic acid (VPCA) that is elaborated and embedded within the final product structures of lincomycin, anthramycin, sibiromycin, tomaymycin and hormaomycin. Using the VPCA mini‐pathway as a starting point, we searched sequence space to identify novel natural product pathways containing a VPCA synthon. From among these novel natural product pathways, representative L‐DOPA dioxygenase gene products from Streptomyces hygroscopicus subsp. jinggangensis and Nocardia arthriditis were studied as pure proteins for their stability and activity on L‐DOPA and related catechols in steady‐state assays for catechol cleavage. These results were analyzed in comparison to characterized L‐DOPA dioxygenases from Streptomyces lincolnensis and Streptomyces sclerotialus.
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